CA3034701A1 - Production of seleno-biologics in genomically recoded organisms - Google Patents
Production of seleno-biologics in genomically recoded organisms Download PDFInfo
- Publication number
- CA3034701A1 CA3034701A1 CA3034701A CA3034701A CA3034701A1 CA 3034701 A1 CA3034701 A1 CA 3034701A1 CA 3034701 A CA3034701 A CA 3034701A CA 3034701 A CA3034701 A CA 3034701A CA 3034701 A1 CA3034701 A1 CA 3034701A1
- Authority
- CA
- Canada
- Prior art keywords
- protein
- variant form
- sequence
- residues
- selenocysteine
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 229960000074 biopharmaceutical Drugs 0.000 title description 17
- 238000004519 manufacturing process Methods 0.000 title description 7
- 238000000034 method Methods 0.000 claims abstract description 61
- 235000016491 selenocysteine Nutrition 0.000 claims abstract description 51
- FDKWRPBBCBCIGA-UWTATZPHSA-N D-Selenocysteine Natural products [Se]C[C@@H](N)C(O)=O FDKWRPBBCBCIGA-UWTATZPHSA-N 0.000 claims abstract description 48
- ZKZBPNGNEQAJSX-UHFFFAOYSA-N selenocysteine Natural products [SeH]CC(N)C(O)=O ZKZBPNGNEQAJSX-UHFFFAOYSA-N 0.000 claims abstract description 48
- 229940055619 selenocysteine Drugs 0.000 claims abstract description 48
- 108090000623 proteins and genes Proteins 0.000 claims description 145
- 102000004169 proteins and genes Human genes 0.000 claims description 141
- 235000018102 proteins Nutrition 0.000 claims description 138
- 125000001554 selenocysteine group Chemical group [H][Se]C([H])([H])C(N([H])[H])C(=O)O* 0.000 claims description 78
- 108020004566 Transfer RNA Proteins 0.000 claims description 55
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 55
- 108020004485 Nonsense Codon Proteins 0.000 claims description 44
- FDKWRPBBCBCIGA-REOHCLBHSA-N (2r)-2-azaniumyl-3-$l^{1}-selanylpropanoate Chemical compound [Se]C[C@H](N)C(O)=O FDKWRPBBCBCIGA-REOHCLBHSA-N 0.000 claims description 39
- 230000001580 bacterial effect Effects 0.000 claims description 37
- 108020004705 Codon Proteins 0.000 claims description 32
- 238000013519 translation Methods 0.000 claims description 32
- 238000000338 in vitro Methods 0.000 claims description 31
- 235000018417 cysteine Nutrition 0.000 claims description 30
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 29
- 150000007523 nucleic acids Chemical class 0.000 claims description 21
- 108020005098 Anticodon Proteins 0.000 claims description 19
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 16
- 108020004707 nucleic acids Proteins 0.000 claims description 14
- 102000039446 nucleic acids Human genes 0.000 claims description 14
- 230000001225 therapeutic effect Effects 0.000 claims description 13
- 238000013518 transcription Methods 0.000 claims description 13
- 230000035897 transcription Effects 0.000 claims description 13
- 241000124008 Mammalia Species 0.000 claims description 10
- 238000012258 culturing Methods 0.000 claims description 10
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical class N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 claims description 10
- 239000011541 reaction mixture Substances 0.000 claims description 10
- 230000000069 prophylactic effect Effects 0.000 claims description 9
- 238000012360 testing method Methods 0.000 claims description 8
- 108020005038 Terminator Codon Proteins 0.000 claims description 7
- 241000894006 Bacteria Species 0.000 claims description 5
- 230000009870 specific binding Effects 0.000 claims description 5
- 238000006467 substitution reaction Methods 0.000 claims description 5
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical class C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 claims description 4
- 230000000295 complement effect Effects 0.000 claims description 3
- 239000001963 growth medium Substances 0.000 claims description 3
- 101000976075 Homo sapiens Insulin Proteins 0.000 claims description 2
- 238000001990 intravenous administration Methods 0.000 claims description 2
- 230000001629 suppression Effects 0.000 claims description 2
- 238000010998 test method Methods 0.000 claims description 2
- 238000003306 harvesting Methods 0.000 claims 1
- 235000001014 amino acid Nutrition 0.000 abstract description 18
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 17
- 108090000765 processed proteins & peptides Proteins 0.000 abstract description 17
- 229920001184 polypeptide Polymers 0.000 abstract description 16
- 150000002019 disulfides Chemical class 0.000 abstract description 9
- 150000003959 diselenides Chemical class 0.000 abstract description 7
- 210000002966 serum Anatomy 0.000 abstract description 7
- -1 selenocysteine amino acids Chemical class 0.000 abstract description 6
- 230000009467 reduction Effects 0.000 abstract description 4
- 238000009776 industrial production Methods 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 17
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 16
- 150000001413 amino acids Chemical class 0.000 description 16
- 238000010348 incorporation Methods 0.000 description 13
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 9
- 230000014616 translation Effects 0.000 description 9
- 230000006870 function Effects 0.000 description 8
- 230000002068 genetic effect Effects 0.000 description 7
- 108700028939 Amino Acyl-tRNA Synthetases Proteins 0.000 description 6
- 102000052866 Amino Acyl-tRNA Synthetases Human genes 0.000 description 6
- 241000588724 Escherichia coli Species 0.000 description 6
- 230000014509 gene expression Effects 0.000 description 6
- 238000013459 approach Methods 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 239000003638 chemical reducing agent Substances 0.000 description 5
- 125000002228 disulfide group Chemical group 0.000 description 5
- 238000012986 modification Methods 0.000 description 5
- 230000004048 modification Effects 0.000 description 5
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 4
- 125000003130 L-selenocysteinyl group Chemical group O=C([*])[C@@](N([H])[H])([H])C([H])([H])[Se][H] 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 230000027455 binding Effects 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- XIMIGUBYDJDCKI-UHFFFAOYSA-N diselenium Chemical compound [Se]=[Se] XIMIGUBYDJDCKI-UHFFFAOYSA-N 0.000 description 4
- 229940022353 herceptin Drugs 0.000 description 4
- 238000002703 mutagenesis Methods 0.000 description 4
- 231100000350 mutagenesis Toxicity 0.000 description 4
- 238000006722 reduction reaction Methods 0.000 description 4
- JULROCUWKLNBSN-UHFFFAOYSA-N seleno-DL-cystine Natural products OC(=O)C(N)C[Se][Se]CC(N)C(O)=O JULROCUWKLNBSN-UHFFFAOYSA-N 0.000 description 4
- 235000020183 skimmed milk Nutrition 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 229960005486 vaccine Drugs 0.000 description 4
- 102000008096 B7-H1 Antigen Human genes 0.000 description 3
- 108010074708 B7-H1 Antigen Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 3
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 3
- 102000004877 Insulin Human genes 0.000 description 3
- 108090001061 Insulin Proteins 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 229920001213 Polysorbate 20 Polymers 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 210000000805 cytoplasm Anatomy 0.000 description 3
- 210000000172 cytosol Anatomy 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 229940125396 insulin Drugs 0.000 description 3
- 230000000813 microbial effect Effects 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 230000014425 selenocysteine incorporation Effects 0.000 description 3
- 150000003345 selenocysteines Chemical class 0.000 description 3
- 238000001228 spectrum Methods 0.000 description 3
- 229930101283 tetracycline Natural products 0.000 description 3
- 239000013598 vector Substances 0.000 description 3
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 2
- YQUVCSBJEUQKSH-UHFFFAOYSA-N 3,4-dihydroxybenzoic acid Chemical compound OC(=O)C1=CC=C(O)C(O)=C1 YQUVCSBJEUQKSH-UHFFFAOYSA-N 0.000 description 2
- 102100021935 C-C motif chemokine 26 Human genes 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 108700039887 Essential Genes Proteins 0.000 description 2
- 101000897493 Homo sapiens C-C motif chemokine 26 Proteins 0.000 description 2
- 102000002265 Human Growth Hormone Human genes 0.000 description 2
- 108010000521 Human Growth Hormone Proteins 0.000 description 2
- 239000000854 Human Growth Hormone Substances 0.000 description 2
- BUGBHKTXTAQXES-UHFFFAOYSA-N Selenium Chemical compound [Se] BUGBHKTXTAQXES-UHFFFAOYSA-N 0.000 description 2
- 108010074686 Selenoproteins Proteins 0.000 description 2
- 102000008114 Selenoproteins Human genes 0.000 description 2
- 238000013019 agitation Methods 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- FPPNZSSZRUTDAP-UWFZAAFLSA-N carbenicillin Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)C(C(O)=O)C1=CC=CC=C1 FPPNZSSZRUTDAP-UWFZAAFLSA-N 0.000 description 2
- 229960003669 carbenicillin Drugs 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
- 229960005091 chloramphenicol Drugs 0.000 description 2
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 229940088598 enzyme Drugs 0.000 description 2
- 230000007717 exclusion Effects 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 238000013467 fragmentation Methods 0.000 description 2
- 238000006062 fragmentation reaction Methods 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 229940127121 immunoconjugate Drugs 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 239000000411 inducer Substances 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 238000001819 mass spectrum Methods 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 108091005573 modified proteins Proteins 0.000 description 2
- 102000035118 modified proteins Human genes 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 230000002018 overexpression Effects 0.000 description 2
- 230000001590 oxidative effect Effects 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- 229910052711 selenium Inorganic materials 0.000 description 2
- 239000011669 selenium Substances 0.000 description 2
- 229940091258 selenium supplement Drugs 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 238000000527 sonication Methods 0.000 description 2
- 230000006641 stabilisation Effects 0.000 description 2
- 238000011105 stabilization Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- OFVLGDICTFRJMM-WESIUVDSSA-N tetracycline Chemical compound C1=CC=C2[C@](O)(C)[C@H]3C[C@H]4[C@H](N(C)C)C(O)=C(C(N)=O)C(=O)[C@@]4(O)C(O)=C3C(=O)C2=C1O OFVLGDICTFRJMM-WESIUVDSSA-N 0.000 description 2
- 238000002849 thermal shift Methods 0.000 description 2
- 238000012384 transportation and delivery Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 208000031295 Animal disease Diseases 0.000 description 1
- 238000012935 Averaging Methods 0.000 description 1
- 101100028791 Caenorhabditis elegans pbs-5 gene Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 102000018997 Growth Hormone Human genes 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- ZFOMKMMPBOQKMC-KXUCPTDWSA-N L-pyrrolysine Chemical compound C[C@@H]1CC=N[C@H]1C(=O)NCCCC[C@H]([NH3+])C([O-])=O ZFOMKMMPBOQKMC-KXUCPTDWSA-N 0.000 description 1
- SHZGCJCMOBCMKK-JFNONXLTSA-N L-rhamnopyranose Chemical compound C[C@@H]1OC(O)[C@H](O)[C@H](O)[C@H]1O SHZGCJCMOBCMKK-JFNONXLTSA-N 0.000 description 1
- PNNNRSAQSRJVSB-UHFFFAOYSA-N L-rhamnose Natural products CC(O)C(O)C(O)C(O)C=O PNNNRSAQSRJVSB-UHFFFAOYSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 229940113231 Neuronal nicotinic receptor antagonist Drugs 0.000 description 1
- 108010049977 Peptide Elongation Factor Tu Proteins 0.000 description 1
- 102000002508 Peptide Elongation Factors Human genes 0.000 description 1
- 108010068204 Peptide Elongation Factors Proteins 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- 108010039491 Ricin Proteins 0.000 description 1
- 101710184528 Scaffolding protein Proteins 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108010030161 Serine-tRNA ligase Proteins 0.000 description 1
- 102100040597 Serine-tRNA ligase, mitochondrial Human genes 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- 101710137500 T7 RNA polymerase Proteins 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 102100036407 Thioredoxin Human genes 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 229940050528 albumin Drugs 0.000 description 1
- DLRVVLDZNNYCBX-CAPXFGMSSA-N allolactose Chemical compound O[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@@H]1OC[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](O)O1 DLRVVLDZNNYCBX-CAPXFGMSSA-N 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 230000001064 anti-interferon Effects 0.000 description 1
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 1
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- XPOORPQJSFUEGJ-UHFFFAOYSA-N bis(selanylidene)-lambda4-sulfane Chemical compound [Se]S[Se] XPOORPQJSFUEGJ-UHFFFAOYSA-N 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 125000001314 canonical amino-acid group Chemical group 0.000 description 1
- 210000004671 cell-free system Anatomy 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000001427 coherent effect Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 150000001945 cysteines Chemical class 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 1
- 229910000396 dipotassium phosphate Inorganic materials 0.000 description 1
- 235000019797 dipotassium phosphate Nutrition 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- BVTBRVFYZUCAKH-UHFFFAOYSA-L disodium selenite Chemical compound [Na+].[Na+].[O-][Se]([O-])=O BVTBRVFYZUCAKH-UHFFFAOYSA-L 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 238000000132 electrospray ionisation Methods 0.000 description 1
- 230000002124 endocrine Effects 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 102000035175 foldases Human genes 0.000 description 1
- 108091005749 foldases Proteins 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 230000005484 gravity Effects 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 238000007917 intracranial administration Methods 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007913 intrathecal administration Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000004895 liquid chromatography mass spectrometry Methods 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000012531 mass spectrometric analysis of intact mass Methods 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 238000006303 photolysis reaction Methods 0.000 description 1
- 102000054765 polymorphisms of proteins Human genes 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000019525 primary metabolic process Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000012846 protein folding Effects 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 238000003753 real-time PCR Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 101150029855 selB gene Proteins 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 108091006024 signal transducing proteins Proteins 0.000 description 1
- 102000034285 signal transducing proteins Human genes 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229960001471 sodium selenite Drugs 0.000 description 1
- 239000011781 sodium selenite Substances 0.000 description 1
- 235000015921 sodium selenite Nutrition 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 108700020534 tetracycline resistance-encoding transposon repressor Proteins 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 229940126622 therapeutic monoclonal antibody Drugs 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 108060008226 thioredoxin Proteins 0.000 description 1
- 229940094937 thioredoxin Drugs 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 102000003390 tumor necrosis factor Human genes 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/22—Hormones
- A61K38/28—Insulins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/61—Growth hormone [GH], i.e. somatotropin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/62—Insulins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/16—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from plants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/241—Tumor Necrosis Factors
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/243—Colony Stimulating Factors
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/249—Interferons
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2863—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for growth factors, growth regulators
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/32—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against translation products of oncogenes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/10—Immunoglobulins specific features characterized by their source of isolation or production
- C07K2317/14—Specific host cells or culture conditions, e.g. components, pH or temperature
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/622—Single chain antibody (scFv)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/94—Stability, e.g. half-life, pH, temperature or enzyme-resistance
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Immunology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Endocrinology (AREA)
- Diabetes (AREA)
- Wood Science & Technology (AREA)
- Gastroenterology & Hepatology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Toxicology (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Epidemiology (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Emergency Medicine (AREA)
- Hematology (AREA)
- Obesity (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Oncology (AREA)
- Botany (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201662381316P | 2016-08-30 | 2016-08-30 | |
| US62/381,316 | 2016-08-30 | ||
| US201762537986P | 2017-07-28 | 2017-07-28 | |
| US62/537,986 | 2017-07-28 | ||
| PCT/US2017/049354 WO2018045018A1 (en) | 2016-08-30 | 2017-08-30 | Production of seleno-biologics in genomically recoded organisms |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA3034701A1 true CA3034701A1 (en) | 2018-03-08 |
Family
ID=61301655
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA3034701A Pending CA3034701A1 (en) | 2016-08-30 | 2017-08-30 | Production of seleno-biologics in genomically recoded organisms |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US11492650B2 (enExample) |
| EP (1) | EP3506945A4 (enExample) |
| JP (2) | JP7186400B2 (enExample) |
| CN (1) | CN109803679A (enExample) |
| CA (1) | CA3034701A1 (enExample) |
| WO (1) | WO2018045018A1 (enExample) |
Families Citing this family (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9840553B2 (en) | 2014-06-28 | 2017-12-12 | Kodiak Sciences Inc. | Dual PDGF/VEGF antagonists |
| WO2017117464A1 (en) | 2015-12-30 | 2017-07-06 | Kodiak Sciences Inc. | Antibodies and conjugates thereof |
| US11542332B2 (en) | 2016-03-26 | 2023-01-03 | Bioatla, Inc. | Anti-CTLA4 antibodies, antibody fragments, their immunoconjugates and uses thereof |
| CN109844105A (zh) | 2016-07-11 | 2019-06-04 | 得克萨斯州大学系统董事会 | 包含硒代半胱氨酸的重组多肽及其产生方法 |
| BR112020017872A2 (pt) | 2018-03-02 | 2020-12-22 | Kodiak Sciences Inc. | Anticorpos de il-6 e construtos de fusão e conjugados dos mesmos |
| JP7384906B2 (ja) * | 2018-07-09 | 2023-11-21 | ジーアールオー・バイオサイエンシズ・インコーポレイテッド | 非標準アミノ酸含有組成物とその使用 |
| CN114144426A (zh) * | 2019-04-19 | 2022-03-04 | 印地安纳大学理事会 | 餐时或基础胰岛素类似物通过内部二硒桥的稳定化 |
| WO2021072265A1 (en) | 2019-10-10 | 2021-04-15 | Kodiak Sciences Inc. | Methods of treating an eye disorder |
| AU2020398327A1 (en) | 2019-12-03 | 2022-07-14 | Evotec International Gmbh | Interferon-associated antigen binding proteins and uses thereof |
| US11179473B2 (en) | 2020-02-21 | 2021-11-23 | Silverback Therapeutics, Inc. | Nectin-4 antibody conjugates and uses thereof |
| CN113512116B (zh) * | 2020-04-10 | 2022-09-20 | 苏州普乐康医药科技有限公司 | 一种抗igf-1r抗体及其应用 |
| JP2023545520A (ja) | 2020-10-14 | 2023-10-30 | ビリジアン セラピューティクス， インコーポレイテッド | 甲状腺眼疾患を治療するための組成物及び方法 |
| WO2023019171A1 (en) | 2021-08-10 | 2023-02-16 | Viridian Therapeutics, Inc. | Compositions, doses, and methods for treatment of thyroid eye disease |
| CN118076644A (zh) * | 2021-09-30 | 2024-05-24 | 正大天晴药业集团股份有限公司 | 针对免疫检查点的双特异性抗体 |
Family Cites Families (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6849417B1 (en) * | 1998-04-06 | 2005-02-01 | The United States Of America As Represented By The Department Of Health And Human Services | Mammalian selenoprotein differentially expressed in tumor cells |
| AU6987200A (en) | 1999-08-16 | 2001-03-13 | Karolinska Innovations Ab | Methods and means for selenoprotein expression |
| WO2007075438A2 (en) * | 2005-12-15 | 2007-07-05 | Codon Devices, Inc. | Polypeptides comprising unnatural amino acids, methods for their production and uses therefor |
| WO2009043051A2 (en) | 2007-09-27 | 2009-04-02 | Biogen Idec Ma Inc. | Cd23 binding molecules and methods of use thereof |
| KR101656107B1 (ko) * | 2007-11-20 | 2016-09-08 | 암브룩스, 인코포레이티드 | 변형된 인슐린 폴리펩티드 및 이의 용도 |
| AU2012216723B2 (en) * | 2007-11-20 | 2014-08-28 | Ambrx, Inc. | Modified insulin polypeptides and their uses |
| JP5572972B2 (ja) * | 2009-03-16 | 2014-08-20 | Ｊｎｃ株式会社 | インスリン分泌促進剤などの薬物のスクリーニング方法 |
| US20140024592A1 (en) * | 2010-09-08 | 2014-01-23 | Howard Florey Institute Of Experimental Physiology And Medicine | Modified Relaxin Polypeptides |
| MX2013008736A (es) * | 2011-01-28 | 2013-11-22 | Ca Nat Research Council | Diseño de dominios de inmunoglobulina. |
| DK2717898T3 (en) | 2011-06-10 | 2019-03-25 | Bioverativ Therapeutics Inc | COAGULATING COMPOUNDS AND PROCEDURES FOR USE THEREOF |
| US10240158B2 (en) | 2011-07-11 | 2019-03-26 | Yale University | Compositions and methods for making selenocysteine containing polypeptides |
| US9464288B2 (en) | 2011-07-11 | 2016-10-11 | Yale University | Compositions and methods for making selenocysteine containing polypeptides |
| US10876142B2 (en) | 2011-07-11 | 2020-12-29 | Yale University | Compositions and methods for making selenocysteine containing polypeptides |
| EP2968552B1 (en) | 2013-03-14 | 2020-03-11 | The Scripps Research Institute | Targeting agent antibody conjugates and uses thereof |
| US20150050682A1 (en) | 2013-08-15 | 2015-02-19 | University Of Vermont And State Agricultural College | Direct assay of thioredoxin reductase activity |
| WO2015066543A1 (en) * | 2013-11-01 | 2015-05-07 | Board Of Regents, The University Of Texas System | Targeting her2 and her3 with bispecific antibodies in cancerous cells |
| US10118950B2 (en) | 2014-08-30 | 2018-11-06 | Northwestern University | Platforms for cell-free protein synthesis comprising extracts from genomically recoded E. coli strains having genetic knock-out mutations in release factor 1 (RF-1) and endA |
| WO2016172269A2 (en) * | 2015-04-20 | 2016-10-27 | University Of Utah Research Foundation | Insulin analogs having shortened b chain peptides and associated methods |
| CN105111304B (zh) * | 2015-09-30 | 2018-12-14 | 山东阿华生物药业有限公司 | 重组人胰岛素前体的纯化和酶切转换方法 |
| US10557160B2 (en) | 2015-12-15 | 2020-02-11 | Board Of Regents, The University Of Texas System | Transgenic bacteria with expanded amino acid usage and nucleic acid molecules for use in the same |
| CN109844105A (zh) * | 2016-07-11 | 2019-06-04 | 得克萨斯州大学系统董事会 | 包含硒代半胱氨酸的重组多肽及其产生方法 |
| AU2017298565B2 (en) | 2016-07-22 | 2021-08-19 | The Walter And Eliza Hall Institute Of Medical Research | Insulin analogs |
| IL264330B2 (en) * | 2016-07-22 | 2024-05-01 | Univ Utah Res Found | An insulin analog, pharmaceutical composition comprising it and its uses |
| CN114144426A (zh) | 2019-04-19 | 2022-03-04 | 印地安纳大学理事会 | 餐时或基础胰岛素类似物通过内部二硒桥的稳定化 |
-
2017
- 2017-08-30 CA CA3034701A patent/CA3034701A1/en active Pending
- 2017-08-30 US US16/329,761 patent/US11492650B2/en active Active
- 2017-08-30 CN CN201780053385.XA patent/CN109803679A/zh active Pending
- 2017-08-30 JP JP2019531589A patent/JP7186400B2/ja active Active
- 2017-08-30 WO PCT/US2017/049354 patent/WO2018045018A1/en not_active Ceased
- 2017-08-30 EP EP17847457.3A patent/EP3506945A4/en active Pending
-
2022
- 2022-11-18 JP JP2022184852A patent/JP7378106B2/ja active Active
Also Published As
| Publication number | Publication date |
|---|---|
| JP7378106B2 (ja) | 2023-11-13 |
| EP3506945A1 (en) | 2019-07-10 |
| JP2023015347A (ja) | 2023-01-31 |
| EP3506945A4 (en) | 2020-07-15 |
| WO2018045018A1 (en) | 2018-03-08 |
| WO2018045018A8 (en) | 2018-05-11 |
| CN109803679A (zh) | 2019-05-24 |
| US11492650B2 (en) | 2022-11-08 |
| JP7186400B2 (ja) | 2022-12-09 |
| US20190194713A1 (en) | 2019-06-27 |
| JP2020502104A (ja) | 2020-01-23 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP7378106B2 (ja) | ゲノム的に再コードした生物におけるセレノ－生物製剤の製造 | |
| US20220213500A1 (en) | Expression Process | |
| US10487133B2 (en) | Codon optimization for titer and fidelity improvement | |
| JP7598243B2 (ja) | 抗体発現を最適化するための方法 | |
| US20080081361A1 (en) | Process for production of a recombinant protein and a fusion protein | |
| RS58219B1 (sr) | Rekombinantna bakterijska ćelija domaćina za ekspresiju proteina | |
| CN108040485A (zh) | 用于优化异源多聚体蛋白质复合物的装配和生产的方法 | |
| JP2022544277A (ja) | カスパーゼ－２バリアント | |
| HK40007802A (en) | Production of seleno-biologics in genomically recoded organisms | |
| KR20210079235A (ko) | Whep 도메인 융합에 의한 목적 단백질의 수용성 증진 방법 | |
| JP2004081199A (ja) | 組換え抗体の製造方法 | |
| JPWO2004031243A1 (ja) | タンパク質ポリマー及びその製造方法 | |
| Shayfutdinov et al. | Optimization of RNA Structure Leads to Increased Biosynthesis of E. coli L-asparaginase when its Gene is Overexpressed | |
| JP2001294599A (ja) | 組み換えｂ型肝炎ウィルス表面抗原 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |
Effective date: 20220504 |
|
| EEER | Examination request |
Effective date: 20220504 |
|
| EEER | Examination request |
Effective date: 20220504 |
|
| EEER | Examination request |
Effective date: 20220504 |
|
| EEER | Examination request |
Effective date: 20220504 |